(a)
To determine: The effect of substitution of valine in the place of glutamate at the 6th position of β-chain.
Introduction: The condition where there’s an inadequate amount of red blood cells are present in the body is called “sickle cell anemia.” During the presence of an insufficient amount of red blood cells in the circulatory system leads to the transportation of a deficient amount of oxygen to various parts of the body. In this disease, the red blood cells become rigid and sticky and they shaped like “sickle” or as the “crescent moons.”
(b)
To determine: The specific amino acid which would be less likely like valine in the harm of the hemoglobin if it changed to the glutamate at the 6th position of the β-chain.
Introduction: The condition where there’s an inadequate amount of red blood cells are present in the body is called “sickle cell anemia.” During the presence of an insufficient amount of red blood cells in the circulatory system leads to the transportation of a deficient amount of oxygen to various parts of the body. In this disease, the red blood cells become rigid and sticky and they shaped like “sickle” or as the “crescent moons.”
(c)
To explain: The similarity in the function and structure of proteins after the difference in various points of the sequence of the amino acid.
Introduction: The condition where there’s an inadequate amount of red blood cells are present in the body is called “sickle cell anemia.” During the presence of an insufficient amount of red blood cells in the circulatory system leads to the transportation of a deficient amount of oxygen to various parts of the body. In this disease, the red blood cells become rigid and sticky and they shaped like “sickle” or as the “crescent moons.”
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Becker's World of the Cell (9th Edition)
- Be sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Thr, Phe, Ile (2 equiv), Asp, Cys, Val, Leu, and forms the following fragments when partially hydrolyzed with HCl: Thr-Ile-Phe, Phe-Ile-Asp-Val, and Asp-Val-Cys-Leu.arrow_forwardBe sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Lys, Pro, Tyr, Ile (2 equiv) , Gln, Trp, Phe, and forms the following fragments when partially hydrolyzed with HCl: Lys–Ile-Phe-Pro, Phe-Pro-Gln-Tyr, and Trp-Ile-Lys.arrow_forwardBe sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Val, Met, Asp (2 equiv), Phe, Trp, Ile, Lys, and forms the following fragments when partially hydrolyzed with HCl: Ile-Asp-Phe, Lys-Met-Val-Trp, and Phe-Asp-Lys-Met. Trp Leu Phe Leu Val Lys Gly Tyr Xarrow_forward
- - Keto counterparts. Name the a-ketoacida-ketoacid that is formed by the transamination of each of the following amino acids: Co, a. Alanine b. Leucine c. Aspartate d. Phenylalanine e. Glutamate f. Tyrosinearrow_forwardShape and dimension. (a) Tropomyosin, a 70-kDa muscle protein, is a two-stranded α-helical coiled coil. Estimate the length of the molecule. (b) Suppose that a 40-residue segment of a protein folds into a two-stranded antiparallel β structure with a 4-residue hairpin turn. What is the longest dimension of this motif?arrow_forwardcotton. Which aspect of the structure of cellulose accounts for its strength? Cellulose is an abundant structural polysaccharide found in plant cell walls, wood, and interchain hydrogen bonding between extended molecular chains repeating unit of N-acetylglucosamine a(1→4) linkages between glucose units branches that occur every 12-30 residues forms a helical conformation in water Which of the following is not correct about chitin? fundamental constituent of the exoskeletons of crustaceans, insects, and spiders b) chitin chains form extended ribbons that pack side-by side a) similar to cellulose but with repeating units of N-acetyl-D-glucosamine c) d) found mainly in the liver in humans, making up as much as 10% of liver mass stacked sheets of chitin strands are stabilized by intrastrand, interstrand, and intersheet hydrogen bondsarrow_forward
- No plagiarism please. Use your own words. Thanks. Discuss the preferred locations of different classes of amino acids in transmembrane proteins. Explain the formation of thioether-linked prenyl anchor proteins. Explain the structure of caveolae.arrow_forwardPro-Ser-Ala-Phe-Glu. Draw this peptide at pH 7 and include its stereochemistry.arrow_forward. A nervous polecat. Pyrrolysine (Pyl, O) and Selenocysteine (Sec, U) are two uncommon amino acids. Knowing that these amino acids exists, translate the following amino acid sequence into one – letter code: Thr – Trp – Ile – Thr – Cys – His – Tyr – Leu – Ile – Thr – Thr – Ile – Glu – Phe – Glu – Arg – Arg – Glu – Thr – Ala – Arg – Glu – Asn – Thr – Tyr – Pyl – Sec – Met – Ala – Leu – Phe – Pyl – Tyr.arrow_forward
- an inorganic ion. Such as metal ion, that improves the fit of an enzyme with its substrate is a(n)?arrow_forwardOn the trail of carbons. Tissue culture cells were incubated with glutamine labeled with 15NN in the amide group. Subsequently, IMP was isolated and found to contain some 15N.N. Which atoms in IMP were labeled?arrow_forwardPeptides. 1. Draw the peptide Ala-Glu-Gly-Lys, as it would occur at physiological pH = 7.4. The R groups of Ala and Gly are not acidic or basic, therefore do not have a pka and the charge on these R groups is therefore independent of pH. Glu is acidic and Lys is basic, therefore the charge on these amino acids is pH dependent. The pKas are shown below. pKa N-term = 9.0 C-term = 3.5 Glu4.1 Lys = 10.5 2. Draw a circle around the peptide bonds. 3. Label the C-terminus and the N-terminus. 4. What is the overall charge on the peptide at pH 7.4?arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning